Earticle

초록

영어

The whole cell bioconversion of daidzein were examined for ortho-hydroxylation using
Streptomyces avermitilis MA-4680 and Nocardia species screened from stock cultures. The
major enzymes responsible for the monohydroxylation step are cytochrome P450s. The
cytochrome P450s belong to a family of ubiquitous heme containing monooxygenases and
catalyze diverse reactions, such as hydroxylation, epoxidation, reduction, oxidation, Odemethylation, desulfonation, peroxidation, deamination and dehalogenation reactions.
Among the various reactions of cytochrome P450, hydroxylation with high regio- and stereoselectivity is of special interest for biotechnological applications. To identify monooxygenases which play a key role for the ortho-hydroxylation, 33 and dozens of
cytochrome P450s from Streptomyces avermitilis MA-4680 and Nocardia species were cloned
and examined, respectively, all the genes were constructed in E. coli BL21(DE3) host system
and each P450s was co-expressed with redox proteins, camA (putidaredoxin reductase) and
camB (putidaredoxin) from Pseudomonas putida, to produce ortho-specific
monohydroxylated daidzein(trihydroxyisoflavonoid). The major hydroxylated products of
daidzein were 7,3’,4’-trihydroxyisoflavone, 6,7,4’-trihydroxyisoflavone and 7,8,4’-
trihydroxyisoflavone which were mono-hydroxylated at ortho position of hydroxy group of
daidzein. The target P450s which showed the highest activity among the tested P450s were
prepared for the templates of the in-vitro evolution.

저자

• Byung-Gee Kim [ Professor, Division of Chemical and Biological Engineering Director, Korea Bio-Hub Center in Bio-MAX institute Seoul National University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576